6ksl | pdb_00006ksl

Staphylococcus aureus lipase - S116A inactive mutant

spinqualitylabelsall models 6ksl, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ksl is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BUA, CA, DAO, ZN Activity: Triacylglycerol lipase, with EC number 3.1.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Staphylococcus aureus lipase (SAL), a triacylglycerol esterase, is an important virulence factor and may be a therapeutic target for infectious diseases. Herein, we determined the 3D structure of native SAL, the mutated S116A inactive form, and the inhibitor complex using the anti-obesity drug orlistat to aid in drug development. The determined crystal structures showed a typical alpha/beta hydrolase motif with a dimeric form. Fatty acids bound near the active site in native SAL and inactive S116A mutant structures. We found that orlistat potently inhibits SAL activity, and it covalently bound to the catalytic Ser116 residue. This is the first report detailing orlistat-lipase binding. It provides structure-based information on the production of potent anti-SAL drugs and lipase inhibitors. These results also indicated that orlistat can be repositioned to treat bacterial diseases. Crystal structure of pathogenic Staphylococcus aureus lipase complex with the anti-obesity drug orlistat.,Kitadokoro K, Tanaka M, Hikima T, Okuno Y, Yamamoto M, Kamitani S Sci Rep. 2020 Mar 25;10(1):5469. doi: 10.1038/s41598-020-62427-8. PMID:32214208 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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